>N515DRAFT_0484 N515DRAFT_0484 glutaryl-CoA dehydrogenase
MSARLNPLDLYDVRSLLTDEERMVQDTVGRFVDERVLPIIGDAFDQGRFPKELIPEIAGLGLLGATLPEQYGCAGMNGVSYGLICQELERGDSGLRSFASVQSSLCMYPIYAYGTEEQKLHYLPKMAAGEIIGCFGLTEPHGGSDPANMKTNARKDGGDWIINGAKMWITNGNLAHIAIVWAQTEDGIQGFIVPTDSQGFTAQEVHKKMSLRASVTSALFFDSVRVPEANRLPNVKGLKGPLGCLTQARYGITWGPIGAAQACLKEVLDYTQERVLFGRPLASNQAIQLKLAEMARRITMAQLLSLQLGRLKDAGNMQPTQVSLAKWNNCRIAIDIARECRDILGGAGITTEHVAIRHALNLESVITYEGTETVHQLVVGRELTGINAF
>biolip__2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
MLDFYALEDLLTPEEKEVQKAARRFLEKEALPHIRDWWEEGVFPTHLIPRFAELGFLGPTLPPEYGGAGVSSAAYGLICYELERVDSGLRSFVSVQSSLVMYPIYAYGSEEQKREFLPKLARGEMVGCFGLTEPDGGSDPYGNMKTRARRDTWVLNGTKMWITNGNLAHLAVIWAKDEVLGFLVPTDTPGFQAREVKRKMSLRASVTSELVLEEVRVPESLRLPKALGLKAPLSCLTQARFGIAWGAMGALEAVYEEAVAFAKSRSTFGEPLAKKQLVQAKLAEMLAWHTEGLLLAWRLARLKDEGKLTPAQVSLAKRQNVWKALQAARMARDILGGSGITLEYHAIRHMLNLETVYTYEGTHDVHTLVLGREITGLNAF
>biolip__3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2
KSTYAPLELFDTDRLLDQDERDIAATVRQFVDTRLKPNVEGWFESATLPSELAKEFGNLGVLGMHLQGYGCAGTNAVSYGLACMELEAGDSGFRSFVSVQGSLSMFSIYRYGSEEQKNEWLPRLAAGDAIGCFGLTEPDFGSNPAGMRTRARRDGSDWILNGTKMWITNGNLADVATVWAQTDDGIRGFLVPTDTPGFTANEIHRKLSLRASVTSELVLDNVRLPASAQLPLAEGLSAPLSCLNEARFGIVFGALGAARDSLETTIAYTQSREVFDKPLSNYQLTQEKLANMTVELGKGMLLAIHLGRIKDAEGVRPEQISLGKLNNVREAIAIARECRTLLGGSGITLEYSPLRHANNLESVLTYEGTSEMHLLSIGKALTGKAAFR
>biolip__3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis
RRGADDLIGINAVLSAEEREIRDTVRSVVQRRIKPHIASWYEDGELPARELAVELGELGLLGMHLKGYGCAGMSAVAYGLACLELEAGDSGIRSLVSVQGSLAMYAIHAFGSDEQKDQWLPDMASGHRIGCFGLTEPDHGSDPAGMRTRATRSGDDWILTGTKMWITNGSVADVAVVWARTDEGIRGFVVPTDTPGFTANTIKSKMSLRASVTSELVLDGVRLPDSARLPGATSLGAPLRCLNEARFGIVFGALGAARDCLETALAYACSREQFDRPIGGFQLTQQKLADMTLEYGKGFLLALHLGRQKDAGELAPEQVSLGKLNNVREAIEIARTARTVLGASGITGEYPVMRHANNLESVLTYEGTSEMHTLIIGQALTGVGAFR
>BRENDA__B0EVL5 glutaryl-CoA dehydrogenase (ETF) (EC 1.3.8.6) (Azoarcus sp.)
MATNRVTFDWADPLYLDSQLTDTERMVRDSARAYSQERLLPRVQEAFRHEKTDRAIFNEMGELGLLGATIPEQYGGSGMNYVCYGLIAREVERVDSGYRSMMSVQSSLVMVPINEFGSEETKQKYLPKLATGEWVGCFGLTEPNHGSDPGSMVTRARKVDGGYSLSGAKMWITNSPIADVFVVWAKDDAGDIRGFVLEKGWKGLSAPAIHGKVGLRASITGEIVMDEVFCPEENAFPTVRGLKGPFTCLNSARYGIAWGALGAAEACYETARQYTMDRKQFGRPLAANQLIQKKLADMLTEITLGLQGCLRLGRLKDEGNAPVELTSIMKRNSCGKSLDIARVARDMLGGNGISDEFCIARHLVNLEVVNTYEGTHDIHALILGRAITGLAAFSN
>metacyc__G1G01-166-MONOMER glutaryl-CoA dehydrogenase (EC 1.3.8.6) (Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440))
MVGKASFNWIDPLLLDQQLTEEERMVRDSAYQFAQDKLAPRVLEAFRHEQTDPAIFREMGEVGLLGATIPEQYGGSGLNYVCYGLIAREVERIDSGYRSMMSVQSSLVMVPINEFGTEAQKQKYLPKLASGEWIGCFGLTEPNHGSDPGSMITRARKVDGGYRLTGSKMWITNSPIADVFVVWAKDDAGDIRGFVLEKGWQGLSAPAIHGKVGLRASITGEIVMDNVFVPEENIFPDVRGLKGPFTCLNSARYGISWGALGAAEACWHTARQYTLDRQQFGRPLAANQLIQKKLADMQTEITLALQGCLRLGRMKDEGTAAVEITSIMKRNSCGKALDIARMARDMLGGNGISDEFGVARHLVNLEVVNTYEGTHDVHALILGRAQTGIQAFY
>SwissProt__Q60759 Glutaryl-CoA dehydrogenase, mitochondrial; GCD; EC 1.3.8.6 (Mus musculus (Mouse))
MSLRGVSARLLSRRSGLRFPRFPRTWSSAAAHTEKTQIRPAKSSRPVFDWKDPLILEEQLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTLSGTKTWITNSPVADLFIVWARCEDNCIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTVGK
>SwissProt__Q92947 Glutaryl-CoA dehydrogenase, mitochondrial; GCD; EC 1.3.8.6 (Homo sapiens (Human))
MALRGVSVRLLSRGPGLHVLRTWVSSAAQTEKGGRTQSQLAKSSRPEFDWQDPLVLEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTASK
>PDB_2r0n_A The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate
EFDWQDPLVLEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLL
ARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTL
NGTKTWITNSPMADLFVVWARCEDGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGP
FGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEM
VSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTA
>PDB_1sir_A The crystal structure and mechanism of human glutaryl-coa dehydrogenase
EFDWQDPLVLEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLL
ARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTL
NGTKTWITNSPMADLFVVWARCEDGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGP
FGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEM
VSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTA
>biolip__2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate
EFDWQDPLVLEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYDGTHDIHALILGRAITGIQAFTA
>SwissProt__P81140 Glutaryl-CoA dehydrogenase, mitochondrial; GCD; EC 1.3.8.6 (Sus scrofa (Pig))
KGGKTQGRSAKSSRPEFDWRDPLVLEEQLTADEILIRDTFRTYCQEHLMPRIVLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQQQQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRALHNPSNRSYTLNGAKTWITNSPVADLFVVWARCEDNCIRGFLLEKGMRGLSAPKIEGKFSLRASATGMIIMDDVEVPEENVLPKASSLAVPFGCLNNARYGISWGVLGAAEFCLHTARQYTLDRIQFGVPLAKNQLIQRKLADMLTEITLGLHACLQLGRLKDQDKVTPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTTDK
>BRENDA__Q3JP94 glutaryl-CoA dehydrogenase (ETF) (EC 1.3.8.6) (Burkholderia pseudomallei)
MAAATFHWDDPLLLDQQLADDERMVRDAAHAYAQGKLAPRVTEAFRHETTDAAIFREMGEIGLLGPTIPEQYGGPGLDYVSYGLIAREVERVDSGYRSMMSVQSSLVMVPIFEFGSDAQKEKYLPKLATGEWIGCFGLTEPNHGSDPGSMVTRARKVPGGYSLSGSKMWITNSPIADVFVVWAKLDEDGRDEIRGFILEKGCKGLSAPAIHGKVGLRASITGEIVLDEAFVPEENILPHVKGLRGPFTCLNSARYGIAWGALGAAESCWHIARQYVLDRKQFGRPLAANQLIQKKLADMQTEITLGLQGVLRLGRMKDEGTAAVEITSIMKRNSCGKALDIARLARDMLGGNGISDEFGVARHLVNLEVVNTYEGTHDIHALILGRAQTGIQAFF
>biolip__3gqtC Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4- tetrahydroquinoxalin-6-yl)methylamine
ATFHWDDPLLLDQQLADDERMVRDAAHAYAQGKLAPRVTEAFRHETTDAAIFREMGEIGLLGPTIPEQYGGPGLDYVSYGLIAREVERVDSGYRSMMSVQSSLVMVPIFEFGSDAQKEKYLPKLATGEWIGCFGLTEPNHGSDPGSMVTRARKVPGGYSLSGSKMWITNSPIADVFVVWAKLDEDGRDEIRGFILEKGCKGLSAPAIHGKVGLRASITGEIVLDEAFVPEENILPHVKGLRGPFTCLNSARYGIAWGALGAAESCWHIARQYVLDRKQFGRPLAANQLIQKKLADMQTEITLGLQGVLRLGRMKDEGTAAVEITSIMKRNSCGKALDIARLARDMLGEFGVARHLVNLEVVNTYEGTHDIHALILGRAQTGIQAF
>PDB_3eon_C 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule
ATFHWDDPLLLDQQLADDERMVRDAAHAYAQGKLAPRVTEAFRHETTDAAIFREMGEIGLLGPTIPEQYGGPGLDYVSYG
LIAREVERVDSGYRSMMSVQSSLVMVPIFEFGSDAQKEKYLPKLATGEWIGCFGLTEPGSMVTRARKVPGGYSLSGSKMW
ITNSPIADVFVVWAKLDEDGRDEIRGFILEKGCKGLSAPAIHGKVGLRASITGEIVLDEAFVPEENILPHVKGLRGPFTC
LNSARYGIAWGALGAAESCWHIARQYVLDRKQFGRPLAANQLIQKKLADMQTEITLGLQGVLRLGRMKDEGTAAVEITSI
MKRNSCGKALDIARLARDMLGGNGDEFGVARHLVNLEVVNTYEGTHDIHALILGRAQTGIQA
>PDB_3gnc_A Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421
AATFHWDDPLLLDQQLADDERMVRDAAHAYAQGKLAPRVTEAFRHETTDAAIFREMGEIGLLGPTIPEQYGGPGLDYVSY
GLIAREVERVDSGYRSMMSVQSSLVMVPIFEFGSDAQKEKYLPKLATGEWIGCFGLTEPMVTRARKVPGGYSLSGSKMWI
TNSPIADVFVVWAKLDEDRDEIRGFILEKGCKGLSAPAIHGKVGLRASITGEIVLDEAFVPEENILPHVKGLRGPFTCLN
SARYGIAWGALGAAESCWHIARQYVLDRKQFGRPLAANQLIQKKLADMQTEITLGLQGVLRLGRMKDEGTAAVEITSIMK
RNSCGKALDIARLARDMLGGNGDEFGVARHLVNLEVVNTYEGTHDIHALILGRAQTGIQA
>PDB_3d6b_C 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei
ATFHWDDPLLLDQQLADDERMVRDAAHAYAQGKLAPRVTEAFRHETTDAAIFREMGEIGLLGPTIPEQYGGPGLDYVSYG
LIAREVERVDSGYRSMMSVQSSLVMVPIFEFGSDAQKEKYLPKLATGEWIGCFGLTEPNHGGSMVTRARKVPGGYSLSGS
KMWITNSPIADVFVVWAKLDEDGRDEIRGFILEKGCKGLSAPAIHGKVGLRASITGEIVLDEAFVPEENILPHVKGLRGP
FTCLNSARYGIAWGALGAAESCWHIARQYVLDRKQPLAANQLIQKKLADMQTEITLGLQGVLRLGRMKDEGTAAVEITSI
MKRNSCGKALDIARLARDMLGFGVARHLVNLEVVNTYEGTHDIHALILGRAQTGIQA
>metacyc__MONOMER-17424 short-chain acyl-CoA dehydrogenase monomer (EC 1.3.8.1) (Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440))
MLVNDEQQQIADAVRAFAQERLKPFAEQWDKDHRFPKEAIDEMAELGLFGMLVPEQWGGSDTGYVAYAMALEEIAAGDGACSTIMSVHNSVGCVPILRFGNEQQKEQFLTPLATGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGSKQFITSGQNAGVVIVFAVTDPEAGKRGISAFIVPTDSPGYQVARVEDKLGQHASDTCQIVFDNVQVPVANRLGAEGEGYKIALANLEGGRIGIASQAVGMARAAFEVARDYANERQSFGKPLIEHQAVAFRLADMATKISVARQMVLHAAALRDAGRPALVEASMAKLFASEMAEKVCSDALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVIARNL
>biolip__4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
HMDELYTEDQRMIRDAARAFATEMLAPNAAQWDHDAHLPDAIVAQLGELGLLGMIVPQELGGSYTDYVAYALAMEEVAAGDAACATMMSVHNSVGCGPILGFGTPAQKDRWLADMAAGRVIGAFCLTEPHAGSEANNLRTRAELRDGQWVLNGAKQFVTNGQRAGVAIVFAMTDPEAGKRGISAFLVPTDTPGFIVGKPEKKMGIRASDTCPITFENCAIPEDNLLGNRGEGLKIALSNLEGGRIGIAAQALGIARAAFDKARRYAGERVQFGKPIAEHQAIQQKLADMAVQINAARLLVHHAAKLRTAGLPCLSEASQAKLFASEMAERVCSDAIQIHGGYGYLVDYEVERHYRDARITQIYEGTSEVQRMVIARQL
>reanno__pseudo13_GW456_L13_PfGW456L13_2983 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens GW456-L13)
MIPNDDQQQIRDMARDFAQERLKPFAAEWDREHRFPKEAIGEMAGLGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILNYGTDEQKERFLKPLASGAMLGAFALTEPQAGSDASGLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVKVPLANRLGEEGEGYRIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSSALQTLGGYGYLNDFPVERIYRDVRVCQIYEGTSDIQRMVISRNL
>SwissProt__P45867 Acyl-CoA dehydrogenase; EC 1.3.99.- (Bacillus subtilis (strain 168))
MNFSLSEEHEMIRKLVRDFAKHEVAPTAAERDEQERFDRELFREMANLGLTGIPWPEDYGGIGSDYLAYVIAVEELSKVCASTGVTLSAHISLCSWPLFAFGTEEQKTEYLTQLALGEKIGAFALTEAGSGSDAGSMKTTAERIGDDYVLNGSKVFITNGGVADIYIVFAVTDPEKKKKGVTAFIVEKDFEGFFTGKKEKKLGIRSSPTTEIMFEDCVVPASKRLGEEGEGFKIAMKTLDGGRNGIAAQAVGIAQGALDAALQYAKERKQFGKSIAEQQGIAFKLADMATMIEASRLLTYQAAWLESSGLPYGKASAMSKLMAGDTAMKVTTEAVQIFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLAD
>biolip__2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4
KSSYFDLPPMEMSVAFPQATPASTFPPCTSDYYHFNDLLTPEEQAIRKKVRECMEKEVAPIMTEYWEKAEFPFHITPKLGAMGVAGGSIKGYGCPGLSITANAIATAEIARVDASCSTFILVHSSLGMLTIALCGSEAQKEKYLPSLAQLNTVACWALTEPDNGSDASGLGTTATKVEGGWKINGQKRWIGNSTFADLLIIFARNTTTNQINGFIVKKDAPGLKATKIPNKIGLRMVQNGDILLQNVFVPDEDRLPGVNSFQDTSKVLAVSRVMVAWQPIGISMGIYDMCHRYLKERKQFGAPLAAFQLNQQKLVQMLGNVQAMFLMGWRLCKLYETGQMTPGQASLGKAWISSKARETASLGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINTLVTGREVTGIASFKPAT
>metacyc__AT3G51840-MONOMER 4-hydroxybutanoyl-CoA oxidase (EC 1.3.3.6) (Arabidopsis thaliana)
MAVLSSADRASNEKKVKSSYFDLPPMEMSVAFPQATPASTFPPCTSDYYHFNDLLTPEEQAIRKKVRECMEKEVAPIMTEYWEKAEFPFHITPKLGAMGVAGGSIKGYGCPGLSITANAIATAEIARVDASCSTFILVHSSLGMLTIALCGSEAQKEKYLPSLAQLNTVACWALTEPDNGSDASGLGTTATKVEGGWKINGQKRWIGNSTFADLLIIFARNTTTNQINGFIVKKDAPGLKATKIPNKIGLRMVQNGDILLQNVFVPDEDRLPGVNSFQDTSKVLAVSRVMVAWQPIGISMGIYDMCHRYLKERKQFGAPLAAFQLNQQKLVQMLGNVQAMFLMGWRLCKLYETGQMTPGQASLGKAWISSKARETASLGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINTLVTGREVTGIASFKPATRSRL
>PDB_2ix5_A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa
KSSYFDLPPMEMSVAFPQATPASTFPPCTSDYYHFNDLLTPEEQAIRKKVRECMEKEVAPIMTEYWEKAEFPFHITPKLG
AMGVAGGSIKGYGCPGLSITANAIATAEIARVDASCSTFILVHSSLGMLTIALCGSEAQKEKYLPSLAQLNTVACWALTE
PDNGSDASGLGTTATKVEGGWKINGQKRWIGNSTFADLLIIFARNTTTNQINGFIVKKDAPGLKATKIPNKIGLRMVQNG
DILLQNVFVPDEDRLPGVNSFQDTSKVLAVSRVMVAWQPIGISMGIYDMCHRYLKERKQFGAPLAAFQLNQQKLVQMLGN
VQAMFLMGWRLCKLYETGQMTPGQASLGKAWISSKARETASLGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINTL
VTGREVTGIASFKPA
>SwissProt__P45857 Acyl-CoA dehydrogenase; EC 1.3.99.- (Bacillus subtilis (strain 168))
MHVTQEQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGIPVPEQYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGNEEQKMKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKNGKYLLNGSKIFITNGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLGLYGSNTTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGIAEAALEHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAADLHNRGLNCGKEASMAKQFASDAAVKAALDAVQIYGGYGYMKDYPVERLLRDAKVTQIYEGTNEIQRLIISKYLLGGT
>reanno__pseudo1_N1B4_Pf1N1B4_4787 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N1B4)
MIPNDEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAGLGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILKFGNDDQKERFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLDGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGITALIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVKVPVANRLGEEGEGYKIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSSALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>reanno__pseudo3_N2E3_AO353_25680 2-methylbutanoyl-CoA dehydrogenase / butanoyl-CoA dehydrogenase / isobutyryl-CoA dehydrogenase (EC 1.3.8.1; EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2E3)
MLPTDEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAELGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILKFGNDDQKERFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLNGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVQVPVANRLGEEGEGYKIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSTALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>reanno__pseudo5_N2C3_1_AO356_26355 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2C3)
MLPTEEQTQIRDMARQFAQERLKPFAAEWDREHRFPREAIAEMAELGFFGMLVPEQWGGCDTGYLAYAMTLEEIAAGDGACSTIMSVHNSVGCVPILKFGNDEQKAKFLTPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEEVKVPVGNRLGEEGEGYKIALANLEGGRVGIAAQAVGMARAAFEAARDYARERSSFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGQPALVEASMAKLFASEMAEKVCSMALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>reanno__pseudo6_N2E2_Pf6N2E2_1146 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2E2)
MLATEEQTQIRDMARQFAEERLKPFAAEWDREHRFPREAIDEMAELGFFGMLVPEQWGGCDTGYLAYAMTLEEIAAGDGACSTIMSVHNSVGCVPILKFGNDEQKAKFLTPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEDLKVPVGNRLGEEGEGYKIALANLEGGRVGIAAQAVGMARAAFEAARDYARERSSFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGQPALVEASMAKLFASEMAEKVCSMALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>reanno__WCS417_GFF2715 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas simiae WCS417)
MLPNEEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAELGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPVLKFGNDQQKEQFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPAAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEDVKVPVANRLGEEGEGYKIALANLEGGRVGIASQAVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSAALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL
>CharProtDB__CH_091788 acyl-CoA dehydrogenase (Bacillus subtilis)
MHVTQEQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGIPVPEQYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGNEEQKMKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKNGKYLLNGSKIFITNGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLGLYGSNTTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGIAEAALEHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAADLHNRGLNCGKEASMAKQFASDAAVKALDAVQIYGGYGYMKDYPVERLLRDAKVTQIYEGTNEIQRLIISKYLLGGT
>biolip__5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
MHVQEQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGIPVPEQYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGNEEQKMKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKNGKYLLNGSKIFITNGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLGLYGSNTTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGIAEAALEHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAADLHNRLNCGKEASMAKQFASDAAVKALDAVQIYGGYGYMKDYPVERLLRDAKVTQIYEGTNEIQRLIISKYLLG
>reanno__psRCH2_GFF2397 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas stutzeri RCH2)
MLPNEDQNAIAEMARQFAQERLKPFAEQWSREHRYPAEAIGEMAALGFFGMLVPEQWGGSDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILRFGNEQQKSDFLTPLARGEQIGAFALTEPQAGSDASSLRTRARRDGDHYVLNGAKQFITSGKHAGTVIVFAVTDPDAGKGGISAFIVPTDSPGYQVVRVEDKLGQHASDTCQIAFEDLRVPVANRLGEEGEGYRIALANLEGGRIGIAAQAVGMARAAFEAARDYARDRETFGKPIIEHQAVAFRLADMATQIAVARQMVHHAAALREVGRPALVEASMAKLFASEMAEKVCSAAIQTLGGYGYLADFPVERIYRDVRVCQIYEGTSDIQRLVISRNLGGPV
>metacyc__MONOMER-21351 butanoyl-CoA dehydrogenase monomer (Eubacterium oxidoreducens)
MDFALTEKHEMARTLFKEFAENEVKPLAQDVDEEERFPVETVEKMAKAGFMGIPIPKEYGGQGCDILTYAMCVEELSKVCGTTGVIVSAHTSLCCDPILTYGTEEQKKKYLPDLAAGKKIGAFGLTEPGAGTDAQGQQTKAVLDGDEWVLNGSKCFITNGSYADVYIVIAVTGKVEKRGRMQKEISAFIVEKGTPGFTFGTKEKKMGIRGSATYELIFQDCRIPKENLLGQKGKGFAVAMHTLDGGRIGIAAQALGLGEGALETTINYVKERKQFGRTISQFQNTQFQLADMATKMQAAQLLVYRAARAKDTQKNYGFEAAQAKLYAAEAAMEVTTKAVQLHGGYGYIREYDVERMMRDAKITEIYEGTSEVQRMVISANLLK
>biolip__7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
LHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>PDB_8sgs_A Short-chain specific acyl-CoA dehydrogenase, mitochondrial
SVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCA
STGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAW
EASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDM
GRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKL
AASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>PDB_7y0b_A Crystal structure of human short-chain acyl-coa dehydrogenase
IYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISR
GCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWIT
NAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQT
LDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAM
AKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>reanno__psRCH2_GFF2392 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas stutzeri RCH2)
MHDLELSEDQRMIRDMARDFARREIAPHAQAWEKAGWIDDTLVAQMGELGLLGMVVPEEWGGSYIDYVAYALAVEEISAGDGATGALMSIHNSVGCGPVLNYGSQAQKDEWLTELASGRAIGCFALTEPQAGSEAHNLRTRAELVDGHWVLNGSKQFCSNAKRSKLAIVFAVTDPELGKKGLSAFLVPTDTPGFAVERSEHKMGIRASDTCGVSLSDCRIPEANLLGERGKGLAIALSNLEGGRIGIGAQALGIARAAFEAALLYARERVQFGKPIAEHQSIANMLADMQTQLNAARLLILHAARLKSAGLPCLSEASQAKLFASEMAEKVCSQAVQIHGGYGYLEDYPVERYYRDARITQIYEGSSEIQRLLIARELANYAL
>metacyc__HS04619-MONOMER short-chain acyl-CoA dehydrogenase monomer (EC 1.3.8.1) (Homo sapiens)
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>BRENDA__Q18AQ1 butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin) (subunit 3/3) (EC 1.3.1.109); short-chain acyl-CoA dehydrogenase (EC 1.3.8.1) (Clostridioides difficile)
MDLNSKKYQMLKELYVSFAENEVKPLATELDEEERFPYETVEKMAKAGMMGIPYPKEYGGEGGDTVGYIMAVEELSRVCGTTGVILSAHTSLGSWPIYQYGNEEQKQKFLRPLASGEKLGAFGLTEPNAGTDASGQQTTAVLDGDEYILNGSKIFITNAIAGDIYVVMAMTDKSKGNKGISAFIVEKGTPGFSFGVKEKKMGIRGSATSELIFEDCRIPKENLLGKEGQGFKIAMSTLDGGRIGIAAQALGLAQGALDETVKYVKERVQFGRPLSKFQNTQFQLADMEVKVQAARHLVYQAAINKDLGKPYGVEAAMAKLFAAETAMEVTTKAVQLHGGYGYTRDYPVERMMRDAKITEIYEGTSEVQRMVISGKLLK
>biolip__4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation
MDFNLTEDQQMIKDMAAEFAEKFLAPTVEERDKAHIWDRKLIDKMGEAGFCGICFPEEYGGMGLDVLSYILAVEELSKVDDGTGITLSANVSLCATPIYMFGTEEQKQKYLAPIAEGTHVGAFGLTEPSAGTDASAQQTTAVLKGDKYILNGSKIFITNGKEADTYVVFAMTDKSQGVHGISAFILEKGMPGFRFGKIEDKMGGHTSITAELIFEDCEVPKENLLGKEGEGFKIAMETLDGGRIGVAAQALGIAEGALAAAVKYSKEREQFGRSISKFQALQFMMADMATKIEAARYLVYHAAMLKNEGKPYSEAAAMAKCFASDVAMEVTTDAVQIFGGYGYTVDYPAERYMRNAKITQIYEGTNQVMRIVTSRALLRD
>PDB_2vig_B Crystal structure of human short-chain acyl coa dehydrogenase
LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTG
VIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEAS
AAVVFASTSISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQAL
GIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>BRENDA__D2RL84 butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin) (subunit 1/3) (EC 1.3.1.109); short-chain acyl-CoA dehydrogenase (subunit 1/2) (EC 1.3.8.1) (Acidaminococcus fermentans)
MDFNLTEDQQMIKDMAAEFAEKFLAPTVEERDKAHIWDRKLIDKMGEAGFCGICFPEEYGGMGLDVLSYILAVEELSKVDDGTGITLSANVSLCATPIYMFGTEEQKQKYLAPIAEGTHVGAFGLTEPSAGTDASAQQTTAVLKGDKYILNGSKIFITNGKEADTYVVFAMTDKSQGVHGISAFILEKGMPGFRFGKIEDKMGGHTSITAELIFEDCEVPKENLLGKEGEGFKIAMETLDGGRIGVAAQALGIAEGALAAAVKYSKEREQFGRSISKFQALQFMMADMATKIEAARYLVYHAAMLKNEGKPYSEAAAMAKCFASDVAMEVTTDAVQIFGGYGYTVDYPAERYMRNAKITQIYEGTNQVMRIVTSRALLRDKKK
>BRENDA__D4QEZ8 short-chain acyl-CoA dehydrogenase (EC 1.3.8.1) (Homo sapiens)
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRDCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>biolip__4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
DDLYTEDQRMILDAARAFCAEVLAPNAAQWDRESHLPDEVVAQMGELGFLGMIVPADWGGSYTDYVAYALALEEIAAGCASCATLVSVHNSVGCGPVLNYGTTEQKERWLRDLASGKTVGAFSLTEPHAGSEAHNLRTRAELRDGKWILNGSKQFVTNGARAGLAIVFAMTDPDEGKRGLSAFVVPTDTPGFIVGKPEKKMGIRASDTCPITLENCAIPQENLLGKRGEGLKIALSNLEGGRIGIAAQATGIARAAFDRARRYARERVQFGKPIAEHQAIAEKLANMATQINAARLLTHHAARLRTAGLPCLSEASQAKLFASEMAEAVCSDAIQIHGGYGFLVDYEVERHYRDARITQIYEGTSEVQRMVIARQL
>metacyc__MONOMER-11693 acyl-CoA dehydrogenase subunit (EC 1.3.8.4; EC 1.3.8.5) (Streptomyces avermitilis)
MDHRLTPELEELRRTVEEFAHDVVAPKIGDFYERHEFPYEIVREMGRMGLFGLPFPEEYGGMGGDYLALGIALEELARVDSSVAITLEAGVSLGAMPIHLFGTDAQKAEWLPRLCSGEILGAFGLTEPDGGSDAGATRTTARLDESTNEWVINGTKCFITNSGTDITGLVTVTAVTGRKPDGKPLISSIIVPSGTPGFTVAAPYSKVGWNASDTRELSFADVRVPAANLLGEQGRGYAQFLRILDEGRIAISALATGLAQGCVDESVKYAGERHAFGRNIGAYQAIQFKIADMEMKAHMARVGWRDAASRLVAGEPFKKEAAIAKLYSSTVAVDNAREATQIHGGYGFMNEYPVARMWRDSKILEIGEGTSEVQRMLIARELGLVG
>reanno__pseudo13_GW456_L13_PfGW456L13_2985 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens GW456-L13)
MHDIELSEEQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGQVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKLAIVFAVTDPDLGKRGISAFLVPTDTAGFIVDRTEHKMGIRASDTCAVTLNNCTIPEANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALAYSRDRVQFGKAINEHQSIANLLADMHMQLNAARLMILHAARLRTAGKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIARELKNYLI
>SwissProt__P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 (Rattus norvegicus (Rat))
MAAALLARAGGSLGRALRARDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
>reanno__ANA3_7024494 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Shewanella sp. ANA-3)
MNSLYTSLNFGLGEEVDMLRDAVQDFAKHEIAPIAAKVDHDNAFPNEIWPVLGGMGLLGVTVPEEYGGANMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQINRNGNAEQKAKYLPKLVSGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDANTYVIYAKTDLTKGAHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDVEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMNACMDIVVPYIHEREQFGKSIGEFQLVQGKLADMYTGMNAAKAYVYSVAKSCDRGETTRKDAAGAILYSAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNESK
>PDB_1jqi_A Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa
VYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISR
GCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWIT
NSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQT
LDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAM
AKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR
>reanno__pseudo3_N2E3_AO353_25670 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas fluorescens FW300-N2E3)
MHDIELTEEQVMIRDMARDFARGEIAPHAQAWEKAGWIDDALVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGALMSIHNSVGCGPVLNYGTEEQKQTWLADLASGQAIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGRRAKLAIVFAVTDPDLGKKGLSAFLVPTDTPGFIVDRSEHKMGIRASDTCAVTLNNCTIPEANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALAYARDRVQFDKPIIEHQSVANMLADMHTRLNAARLLILHAARLRSAGKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVERYYRDARITQIYEGSSEIQRMVIARELKNYLV
>biolip__2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
LTQEQRLVLDAVRRVAREVLYPLAPEYDRKAEYPWPQLKALAELGLLGMTTPEEWGGVGLDSVTWALALEELAAADPSVAVIVSVTSGLPQYMLLRFGSEAQKRRYLVPLARGEWIGAFCLTEPQAGSDAKSLRAEARRVKGGFVLNGVKSWITSAGHAHLYVVMARTEKGISAFLVEKGTPGLSFGRPEEKMGLHAAHTAEVRLEEVFVPEENLLGEEGRGLAYALAGLDSGRVGVAAQAVGIARGAFEIAKAYAEEREQFGKKLKEHQAIAFKIADMHVKIAAARALVLEAARKKDRGERFTLEASAAKLFASAAAVEVTREAVQVLGGYGYHRDYRVERYYRDAKVTEIYEGTSEIQRLVIARELYR
>biolip__7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
TLPKEYQDLRDTVADFARSVVAPVSAKHDEEHSFPYEVVAKMGEMGLFGLPFPEEYGGMGGDYFALALALEELGKVDQSVAITLEAGVGLGAMPIYRFGNEEQKSKWLPDLLAGRALAGFGLTEPGAGSDAGSTRTTARLDGGEWVVNGSKQFITNSGTDITSLVTITAVTKEISTIIVPSGTPGFIVEPVYNKVGWNASDTHPLSFDDARVPEENLLGIRGKGYANFLSILDEGRIAIAALATGVAQGCVDESVKYAKERQSFGQPIGSYQAISFKIARMEARAHVARTAYYEAAAKMLAGKPFKKEAAIAKMISSEAAMDNARDATQVHGGYGFMNEYPVARHYRDSKILEIGEGTTEVQLMLIARSLGL
>metacyc__HS10828-MONOMER Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.5) (Homo sapiens)
MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY
>biolip__2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
APLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY
>SwissProt__Q3ZBF6 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 (Bos taurus (Bovine))
MAATLLARACGLVRGAPWPWGWRRLHTVYQSVELPETHQMLRQTCRDFAEKELFPIAAQVDKEHRFPAAQVKKMGELGLMAMNVPEELSGAGLDYLAYSIAMEEISRGCASTGVIMSVNNSLYLGPILKFGTKEQKQQWVAPFTSGDKIGCFALSEPGNGSDAGAAATTARADGDSWVLSGTKAWITNAWEASAVVVFASTDRSLHNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDRRIPKDSLLGEPGLGFKIAMQTLDTGRIGIASQALGIAQAALDCAVTYAENRSAFGAPLTKLQAIQFKLADMALALESARLLTWRAAMLKDNKKPFTKEAAMAKLAASEAATAITHQAMQILGGMGYVKEMPAERHYRDARITEIYEGTSEIQRLVVAGHLLKSYRS
>reanno__SB2B_6937192 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Shewanella amazonensis SB2B)
MSHLYSTLNFGLGEDVDMLRDAVYEFAKGEIAPLAEKVDRDNAFPNELWAKFGDMGLLGVTVAEEYGGVNMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQIYRNGNEAQRAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDAHTYVIYAKTDLDKGPHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDCEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMTACMDIVVPYVHERVQFGKSIGEFQLVQGKLADMYTGMNAAKSYVYNVARACDRGETTRKDAAGVILYAAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETK
>SwissProt__Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 (Megasphaera elsdenii)
MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGGDVLSYILAVEELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR
>reanno__WCS417_GFF2713 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) (Pseudomonas simiae WCS417)
MQDIEYTEEQVMIRDMARDFARGEIAPYAQAWEKAGWIDDALVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGALMSIHNSVGCGPILNYGTESQKQTWLADLASGQAIGCFCLTEPQAGSEAHNLRTRAELRDGHWVITGAKQFVSNGKRAKLAIVFAITDPELGKKGISAFLVPTATPGFVVDRTEHKMGIRASDTCAVTLNQCTVPEANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALAYARDRVQFDKAIIEHQSVANLLADMQTQLNAARLLILHAARLRSAGKPCLSEASQAKLFASEMAEKVCSSAMQIHGGYGYLEDYPVERYYRDARITQIYEGTSEIQRMVIARELKHYQL
>SwissProt__P52042 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; SCAD; EC 1.3.8.1 (Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787))
MDFNLTREQELVRQMVREFAENEVKPIAAEIDETERFPMENVKKMGQYGMMGIPFSKEYGGAGGDVLSYIIAVEELSKVCGTTGVILSAHTSLCASLINEHGTEEQKQKYLVPLAKGEKIGAYGLTEPNAGTDSGAQQTVAVLEGDHYVINGSKIFITNGGVADTFVIFAMTDRTKGTKGISAFIIEKGFKGFSIGKVEQKLGIRASSTTELVFEDMIVPVENMIGKEGKGFPIAMKTLDGGRIGIAAQALGIAEGAFNEARAYMKERKQFGRSLDKFQGLAWMMADMDVAIESARYLVYKAAYLKQAGLPYTVDAARAKLHAANVAMDVTTKAVQLFGGYGYTKDYPVERMMRDAKITEIYEGTSEVQKLVISGKIFR
>reanno__pseudo3_N2E3_AO353_20350 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas fluorescens FW300-N2E3)
MSYPTLNFALGETIDMLRDQVRAFVSKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGTHEQKAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>reanno__WCS417_GFF3325 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas simiae WCS417)
MSYPSLNFALGETIDMLRDQVQSFVSKEIAPRAAQIDRDNLFPADLWQKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHSQKLKYLPKLISGEHVGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDASTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGTLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>biolip__1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
IDFSLTEEQRQLQALARRFAKEVILPVAQEYDEKEEVPWPVIEKLHEVGLLNAIIPEEYGGMGLKMLDEVIVGEELAYACMGIYTIPMASDLGITPVLLAGTEEQKERFLRPLTEKPALAAFALSEPGNGSDAAALKTRAIRQGDHYVLNGTKMWISNGGEAEWVVVFATVNPELRHKGVVALVVERGTPGFKAIKIHGKMGQRASGTYELVFEDVKVPVENRLGEEGEGFKIAMQTLNKTRIPVAAGSVGVARRALDEARKYAKEREAFGEPIANFQAIQFKLVDMLIGIETARMYTYYAAWLADQGLPHAHASAIAKAYASEIAFEAANQAIQIHGGYGYVREFPVEKLLRDVKLNQIYEGTNEIQRLIIARHILAA
>PDB_1ukw_B Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
IDFSLTEEQRQLQALARRFAKEVILPVAQEYDEKEEVPWPVIEKLHEVGLLNAIIPEEYGGMGLKMLDEVIVGEELAYAC
MGIYTIPMASDLGITPVLLAGTEEQKERFLRPLTEKPALAAFALSEPGNGSDAAALKTRAIRQGDHYVLNGTKMWISNGG
EAEWVVVFATVNPELRHKGVVALVVERGTPGFKAIKIHGKMGQRASGTYELVFEDVKVPVENRLGEEGEGFKIAMQTLNK
TRIPVAAGSVGVARRALDEARKYAKEREAFGEPIANFQAIQFKLVDMLIGIETARMYTYYAAWLADQGLPHAHASAIAKA
YASEIAFEAANQAIQIHGGYGYVREFPVEKLLRDVKLNQIYEGTNEIQRLIIARHILAA
>metacyc__MONOMER-20595 cinnamate reductase monomer (EC 1.3.8.15) (Clostridium sporogenes (strain ATCC 15579))
MFFTEQHELIRKLARDFAEQEIEPIADEVDKTAEFPKEIVKKMAQNGFFGIKMPKEYGGAGADNRAYVTIMEEISRASGVAGIYLSSPNSLLGTPFLLVGTDEQKEKYLKPMIRGEKTLAFALTEPGAGSDAGAVATTAREEGDYYILNGRKTFITGAPISDNIIVFAKTDMSKGTKGITTFIVDSKQEGVSFGKPEDKMGMIGCPTSDIILENVKVHKSDILGELNKGFITAMKTLSVGRIGVAAQALGIAQAAVDEAVKYAKQRKQFNRPIAKFQAIQFKLANMETKLNAAKLLVYNAAYKMDCGEKADKEASMAKYFAAESAIQIVNDALQIHGGYGYIKDYKIERLYRDVRVIAIYEGTSEVQQMVIASNLLK
>reanno__pseudo6_N2E2_Pf6N2E2_2191 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas fluorescens FW300-N2E2)
MSYPSLNFALGETIDMLRDQVQAFVNAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDKYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEDNILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>ENA__AAL09094.1 DcaA (Acinetobacter baylyi)
MIRDEGMLQQLLSTIRDFVKNELIPREHEVAEKDCIPEDIIQQMRELGLFGLTIPEEYGGLGITMEEEVNVAFELGQTSPAFRSLIGTNNGIGSSGLIIDGTEEQKQKYLPRYASGEIIGSFCLTEPEAGSDAASLKTTAVKDGDFYILNGTKRFITNAPHAATFTVMARTNPAIKGAGGISAFLVEANTPGITLGKIDQKMGQKGSHTCDVIFENCRVPASALIGGVEGVGFKTAMKVLDKGRLHIGAYSVGVAERMLNDALHYAVERKQFGQPIANFQLIQAMLADSKAEIYAAKCMVLDAARRRDEGQNISTEASCAKMFATEMCGRVADRCVQIHGGAGYISEYSIERFYRDVRLFRLYEGTTQVQQIIIAKNMIKEVTS
>metacyc__MONOMER-11692 2-methyl branched chain acyl-CoA dehydrogenase subunit (EC 1.3.8.5) (Rattus norvegicus)
MAVSAFQLWRAGGLLRRNFLTHSSSWKIPPRVLKSSQPEALLSVTNNALCFAPLQTFTDEDIMMQKAVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGMMGIEVEAKYGGTEASFLCSVLVIEELAKVDASVALLCDIQNTVINKLFRKHGTEEQKATYLPKLVTEKLGSFCLSEAGAGSDSFALKTRADKSGNYYVINGSKMWISNAEHAELFLVFANVDPPSGYRGITCFLVDRDTEGFQIGRRENKMGIRASSTCQLTFENVKVPETSVLGKIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAHVATQLEAARLLTYNAARLVEAGRPFIKEASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGTSNIQLNTIAKHIDAEY
>reanno__acidovorax_3H11_Ac3H11_2996 2-methyl-branched-chain-enoyl-CoA reductase (EC 1.3.8.5) (Acidovorax sp. GW101-3H11)
MLLTQDQEMIRDAVRDFAQTELWPHAARWDKEHHFPKDAHQGLAALGAYGICVPEEFGGANLDYLTLALVLEEIAAGDGGTSTAISVTNCPVNAILMRYGNAQQKRDWLTPLARGEMLGAFCLTEPHVGSDASALRTTAVKQGDEYVINGVKQFITSGKNGQVAIVIAVTDKGAGKKGMSAFLVPTNNPGYVVARLEDKLGQHSSDTAQINFDNCRIPAENLIGAEGEGYKIALGALEGGRIGIAAQSVGMARSAFDAALAYSKERESFGTAIFNHQAVGFRLADCATQIEAARQLIWHAAALRDAGKPCLKEAAMAKLFASEMAERVCSAAIQTLGGYGVVNDFPVERIYRDVRVCQIYEGTSDVQKIIIQRALA
>reanno__pseudo5_N2C3_1_AO356_01580 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Pseudomonas fluorescens FW300-N2C3)
MSYPSLNFALGETIDMLRDQVQAFVKAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
>SwissProt__Q22347 Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial; MCAD; EC 1.3.8.7 (Caenorhabditis elegans)
MLSRIATSSLGLSRSATGVIATQSRQISFDLSETQKEIQDAALKFSKDVLVPNAAKFDESGEFPWEIVRQAHSLGLMNPQIPEKYGGPGMTTLETALIVEALSYGCTGIQLGIMGPSLAIAPVYISGNEEQKKKYLGALAAEPIIASYCVTEPGAGSDVNGVKTKCEKKGDEYIINGSKAWITGGGHAKWFFVLARSDPNPKTPAGKAFTAFIVDGDTPGITRGKKEKNMGQRCSDTRVITFEDVRVPAENVLGAPGAGFKVAMEAFDMTRPGVAAGALGLSWRCLDESAKYALERKAFGTVIANHQAVQFMLADMAVNLELARLITYKSANDVDNKVRSSYNASIAKCFAADTANQAATNAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRIVISRMLLGHFAQNGTSRI
>SwissProt__Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 (Drosophila melanogaster (Fruit fly))
MAFLNKLAAPALRQLVSQSRAYAAVSHVSPNGTSFALTEDQLQLQELARKFTREEIIPVAAQYDKSGEYPWPIIKKAWELGLMNNHIPADIGGLDLDVFTTCLSAEELAYGCTGIMTALEASGLGQTPVILSGNKEQKKKYLGRLLEEPLVAAYCVTEPGAGSDVSGIKTRAEKKGDEWVINGQKMWITNGGVANWYFVLARTNPDPKCPPSKAFTGFIVERDSPGLTPGRKELNMGQRASDTRGITFEDVRVPKENVLIGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRCLDEALKYALERKTFGVPIAYHQAVQFMLADMAIGVETSRLAWRLSAWEIDQGRRNSYYASIAKCHAADMANKIASDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISRNMYEAAKGQA
>reanno__Smeli_SM_b21121 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) (Sinorhizobium meliloti 1021)
MFEAGLNFALGEEIDALRASVRRFASERIAPLADDADRSNAFPMSLWREMGELGLLGITADEAHGGAGLGYLAHCVAMEEISRASASVGLSYGAHSNLCVNQINRNGKPAQKSRYLPKLISGEHVGALAMSEPGAGSDVVSMKLKADKRGDRYVLNGSKMWITNGPDADVLVVYAKTDPAAGPRGITAFLVEKAFPGFSAGQKLDKLGMRGSNTSELIFTDCEVPEENVLGGVGEGVKVLMSGLDYERVVLSAGPLGIMAACLDVVVPYLHERKQFGQPIGEFQLMQGKLADMYVTMNAARAYVYAVAAACDRGETARKDAAGCILYAAEKATAMALEAIQALGGNGYTNDYPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFAETK
>biolip__2a1tC Structure of the human mcad:etf e165betaa complex
GLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
>metacyc__HS04089-MONOMER mitochondrial medium-chain acyl-CoA dehydrogenase monomer (EC 1.3.8.7) (Homo sapiens)
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
>PDB_1egc_A Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa
LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY
GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN
GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM
GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA
SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDKYKN
>biolip__3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex
MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTEYPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANRKGHHHH
>PDB_3mpj_B Structure of the glutaryl-coenzyme a dehydrogenase
MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIA
RGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWI
SNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFG
SLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDV
AMAKYAAGEAVSKCANYAMRILGAYGYSTEYPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANRKGHH
>SwissProt__C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 (Desulfococcus multivorans)
MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTEYPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANR
>SwissProt__P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 (Sus scrofa (Pig))
MAAMFRRSCRVLRSLSHFGWRSQHTKAVPQCEPGSGFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYGCTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYASIAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYKN
>PDB_3mde_A Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate
GFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYG
CTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG
GKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMG
TFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYAS
IAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYK
>biolip__3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate
GFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYGCTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYASIAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYK
>PDB_1udy_A Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa
GFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYG
CTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG
GKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMG
TFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYAS
IAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYK
>biolip__3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr
HIALREAIRALAEKEIAPYAAEVDEKARFPEEALAALNSSGFSAIHVPEEYGGQGADSVATCIVIEEVARVDCSASLIPAVNKLGTMGLILRGSEELKKQVLPAVASGEAMASYALSEREAGSDAASMRTRAVADGDDWILNGSKCWITNGGKSTWYTVMAVTDPDKGANGISAFMVHKDDEGFTVGPKERKLGIKGSPTTELYFENCRIPGDRIIGEPGTGFKTALATLDHTRPTIGAQAVGIAQGALDAAIAYTKERKQFGRPVSDNQGVQFMLADMAMKIEAARLMVYSAAARAERGDLGFISAASKCFASDVAMEVTTDAVQLFGGYGYTQDFPVERMMRDAKITQIYEGTNQIQRVVMSRALLR
>SwissProt__H6LGM6 Caffeyl-CoA reductase-Etf complex subunit CarC; Caffeoyl-CoA reductase CarC; NADH-dependent caffeyl-CoA reduction; EC 1.3.1.108 (Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1))
MYFSEQNKMIRKLARDFAEKELTTEILDEVEESGEFPQEILDKMAKFGFFGIKIPKSLGGSGGDHMSYVICMEEFARVSGVASVYLSSPNSLAGGPLLLSGTEEQIEKYLKPIITGKKKLAFALTEPGAGSDAGGMSTTAVDMGDYYLLNGRKTFITMAPLCDDAVIYAKTDMSKGTRGISAFIVDLKSEGVSMGKNEHKMGLIGCATSDIIMEDVKVPKENRLGEVNKGFSNAMKTLDVGRLGVASQSIGVAQGALDEAIKYAKERKQFGKRIADFQAIAFMIADMATKLEAAKLLVYNAASLMDNKKNATKEASMAKFYASEICNEICAKAVQIHGGYGYIKEYKVERMYRDCRVFTIYEGTSQVQQMVISGMLLKK
>PDB_8i4r_A Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
FDLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARV
CASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNA
GISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTL
DHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAA
AKCFASDVAMEITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK
>PDB_8i4p_A Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
FDLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARV
CASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNA
GISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTL
DHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAA
AKCFASDVAMEITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK
>biolip__7w0jE Acyl-coa dehydrogenase, tfu_1647
DFDLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAAAKCFASDVAMEITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK
>metacyc__HS03876-MONOMER long-chain-acyl-CoA dehydrogenase monomer (EC 1.3.8.8; EC 1.3.8.7) (Homo sapiens)
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIVFDK
>biolip__4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
MFEAGLNFALGEEIDALRASVRRFASERIAPLADDADRSNAFPMSLWREMGELGLLGITADEAHGGAGLGYLAHCVAMEEISRASASVGLSYGAHSNLCVNQINRNGKPAQKSRYLPKLISGEHVGALAMSEPGVSMKLKADKRGDRYVLNGSKMWITNGPDADVLVVYAKTDPPRGITAFLVEKAFPGFSAGQKLDKLGMRGSNTSELIFTDCEVPEENVLGGVGEGVKVLMSGLDYERVVLSAGPLGIMAACLDVVVPYLHERKQFGQPIGEFQLMQGKLADMYVTMNAARAYVYAVAAACDRGETARKDAAGCILYAAEKATAMALEAIQALGGNGYTNDYPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFAE
>biolip__8sgrA 8sgrA
SLLPVDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFH
>SwissProt__P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 (Homo sapiens (Human))
MAEMATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFH
>PDB_1ivh_A Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity
VDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEE
ISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKF
WITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVY
VLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTA
KDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNAD
>biolip__4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis
ALTAEEETIVKTVHDFVEKQVKPVVRELEHANTYPEELIETMKEIGIFGLAIPEPYGFGAVSMPCYVQVAEELARGWMSLAGAMGGHTVVSKLLLLFGTEEQKQKYLPRMATGELRATMALTEPGGGSDLQAMRTVARRDGDDYVINGSKTWISNARRSDLVALMCKTDPDAQPAHKGVSILLVEKVPGFDVSRDLPKLGYKGVESCELNFTDARVPVSSLLGDDEGRGFAQMMKGLEVGRLQVAARATGVARAAFEDALRYSQERESFGKPIWQHQSVGNMLADMGTKLYAARSLLLSAAEKFDAGQRCDMEAGMAKLFASETAMQIALDAVRVHGGYGYSTEYDVERYFRDAPLMIVGEGTNEIQRNVIAKQLVARGGLDI
>SwissProt__P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 (Mus musculus (Mouse))
MAARLLLRSLRVLKARSAPRPPPSARCSHSGAEARLETPSAKKLTDVGIRRIFSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS
>biolip__2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
TARYLREEHHMFRAAFRKFLEKEAYPHYNDWEKRGIIPRSFWAKMGENGFLCPWVDEKYGGLNADFAYSVVINEELEKVGSSLVGIGLHNDIVTPYIASYGTEEQKQKWLPKCVTGELITAIAMTEPGAGSDLANISTTAVKDGDYYIVNGQKTFITNGIHADLIVVACKTDPQAKPPHRGISLLVVERDTPGFTRGRKLEKVGLHAQDTAELFFQDAKVPAYNLLGEEGKGFYYLMEKLQQERLVVAIAAQTAAEVMFSLTKQYVKQRTAFGKRVSEFQTVQFRLAEMATEIALGRTFVDRVIEEHMAGKQIVTEVSMAKWWITEMAKRVAAEAMQLHGGYGYMEEYEIARRYRDIPVSAIYAGTNEMMKTIIARQLDL
>biolip__2d29A Structural study on project id tt0172 from thermus thermophilus hb8
GLWFEEGAEERQVLGPFREFLKAEVAPGAAERDRTGAFPWDLVRKLAEFGVFGALVPEAYGGAGLSTRLFARMVEAIAYYDGALALTVASHNSLATGHILLAGSEAQKEAFLPKLASGEALGAWGLTEPGSGSDAAALKTKAEKVEGGWRLNGTKQFITQGSVAGVYVVMARTDPPPSPERKHQGISAFAFFRPERGLKVGRKEEKLGLTASDTAQLILEDLFVPEEALLGERGKGFYDVLRVLDGGRIGIAAMAVGLGQAALDYALAYAKGREAFGRPIAEFEGVSFKLAEAATELEAARLLYLKAAELKDAGRPFTLEAAQAKLFASEAAVKACDEAIQILGGYGYVKDYPVERYWRDARLTRIGEGTSEILKLVIARRLLEAV
>biolip__2z1qB Crystal structure of acyl coa dehydrogenase
KKLWQKGGGWLLEVPERVYTPEDFDESVKEIARTTRTFVEREVLPLLERMEHGELELNVPLMRKAGELGLLAIDVPEEYGGLDLPKVISTVVAEELSGSGGFSVTYGAHTSIGTLPLVYFGTEEQKRKYLPKLASGEWIAAYCLTEPGSGSDALAAKTRATLSEDGKHYILNGVKQWISNAGFAHLFTVFAKVDGEHFTAFLVERDTPGLSFGPEEKKMGIKASSTRQVILEDVKVPVENVLGEIGKGHKIAFNVLNVGRYKLGAGAVGGAKRALELSAQYATQRVQFGRPIGRFGLIQQKLGEMASRIYAAESAVYRTVGLIDEALLGKKGPEAVMAGIEEYAVEASIIKVLGSEVLDYVVDEGVQIHGGYGYSQEYPIERAYRDARINRIFEGTNEINRLLIPGMLLRRAEPEDLELHQVQNLKKLALMVAGLAVQKYGQGVEEEQEVLGAVADILIDAYAAESALLRARRLGGLAPVLARIYLAQALDRAQAGALSVLPRLVEGDEARVVYSAARRLTKREPGDLVALRRQAAEAVLEAGGYPIPR
>biolip__3nf4A Crystal structure of acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to flavin adenine dinucleotide
MAVDRLLPSQEAAELIELTREIADKVLDPIVDRHEKDETYPEGVFEQLGAAGLLSLPQPEEWGGGGQPYEVYLQVLEEIAARWASVAVAVSVHSLSSHPLLVFGTEEQKKRWLPGMLSGEQIGAYSLSEPQAGSDAAALRCAATPTDGGYVINGSKSWITHGGKADFYTLFARTGSRGVSCFLVPADQPGLSFGKPEEKMGLHAVPTTSAFYDNARIDADRRIGEEGQGLQIAFSALDSGRLGIAAVATGLAQAALDEAVAYANEKIIDHGLGFLLADMAAAVATARATYLDAARRRDQGRPYSQQASIAKLTATDAAMKVTTDAVQVFGGVGYTRDYRVERYMREAKIMQIFEGTNQIQRLVIARGLT
>biolip__3owaC Crystal structure of acyl-coa dehydrogenase complexed with fad from bacillus anthracis
AVKGGSFLVDEITIDQVFTPEDFSSEHKMIAKTTEDFIVNEVLPELEYLEQHEFDRSVRLLKEAGELGLLGADVPEEYGGIGLDKVSSALIAEKFSRAGGFAITHGAHVGIGSLPIVLFGNEEQKKKYLPLLATGEKLAAYALTEPGSGSDALGAKTTARLNAEGTHYVLNGEKQWITNSAFADVFIVYAKIDGEHFSAFIVEKDYAGVSTSPEEKKMGIKCSSTRTLILEDALVPKENLLGEIGKGHIIAFNILNIGRYKLGVGTVGSAKRAVEISAQYANQRQQFKQPIARFPLIQEKLANMAAKTYAAESSVYRTVGLFESRMSTLSEEEVKDGKAVAASIAEYAIECSLNKVFGSEVLDYTVDEGVQIHGGYGFMAEYEIERMYRDSRINRIFEGTNEINRLIVPGTFLRKAMKGELPLLQKAQKLQEELMMMMPEEVGDEPLALQKYLVNNAKKIGLMVAGLAAQKYGKALDKEQEILVNIADIVSNLYAMESAVLRTEKAIKTTGLEKNKQKVLYTEVFCQEAFNEIEAHAKETLIAVENGDMLRMMLSSLRKLTRHTPLNVIPKKREIAAKILEDERYTV
>PDB_7p9x_A Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa
HLTEEQKLTLDMVRDVATREIAPRALELDEKSLFPEYARDLFAKLGLLNPLLPAAYGGTEMGVLTLALILEELGRVCAST
ALLLIAQTDGMLPIIHGGSPELKERYLRRFAGESTLLTALAATEPAAGSDLLAMKTRAVRQGDKYVINGQKCFITNGSVA
DVIVVYAYTDPEKGSKGISAFVVEKGTPGLVYGRNESKMGMRGSINSELFFENMEVPAENIIGAEGTGFANLMQTLSTNR
VFCAAQAVGIAQGALDIAVRHTQDRVQFGKPIAHLAPVQFMVADMATAVEASRLLTRKAAELLDDGDKKAVLYGSMAKTM
ASDTAMRVTTDAVQVLGGSGYMKENGVERMMRDAKLTQIYTGTNQITRMVTGRALLFP